人迁移抑制因子：纯化及免疫化学特性分析
Human migration inhibitory factor: purification and immunochemical characterization.
作者信息
Block L H, Jaksche H, Bamberger S, Ruhenstroth-Bauer G
出版信息
J Exp Med. 1978 Feb 1;147(2):541-53. doi: 10.1084/jem.147.2.541.
Abstract
Using gel filtration and preparative isotachophoresis, the migration inhibitory factor (MIF) was highly purified from human lymphocytes activated with concanavalin A. MIF is an acidic protein with a mol wt of approximately equal to 25,000 daltons as determined by gel filtration and analytical polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The protein inhibits migration of macrophages in the capillary test and in addition, has a slowing effect on the electrophoretic mobility of guinea pig peritoneal macrophages. Rabbit antibodies specific for this protein, as determined by immunochemical techniques, neutralized the biological effect of MIF on migration and on the electrophoretic mobility of macrophages.
摘要
利用凝胶过滤和制备等速电泳技术，从经伴刀豆球蛋白A激活的人淋巴细胞中高度纯化出迁移抑制因子（MIF）。通过凝胶过滤以及在十二烷基硫酸钠存在下的分析型聚丙烯酰胺凝胶电泳测定，MIF是一种酸性蛋白，分子量约为25,000道尔顿。该蛋白在毛细管试验中可抑制巨噬细胞的迁移，此外，对豚鼠腹腔巨噬细胞的电泳迁移率有减缓作用。通过免疫化学技术测定，针对该蛋白的兔抗体可中和MIF对巨噬细胞迁移和电泳迁移率的生物学效应。
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